4LNO
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: form two of GS-1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-12-23 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 209.860, 138.940, 144.730 |
| Unit cell angles | 90.00, 125.17, 90.00 |
Refinement procedure
| Resolution | 71.680 - 2.900 |
| R-factor | 0.196 |
| Rwork | 0.196 |
| R-free | 0.25600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bvc |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.200 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 71.680 |
| High resolution limit [Å] | 2.900 |
| Number of reflections | 75070 |
| Completeness [%] | 99.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | PEG8000, magnesium chloride, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
